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Parafibromin (Cell division cycle protein 73 homolog) (Hyperparathyroidism 2 protein)

 CDC73_HUMAN             Reviewed;         531 AA.
Q6P1J9; A6NLZ8; B2RBR2; Q6PK51; Q96A07; Q9H245; Q9H5L7;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
20-DEC-2017, entry version 149.
RecName: Full=Parafibromin;
AltName: Full=Cell division cycle protein 73 homolog;
AltName: Full=Hyperparathyroidism 2 protein;
Name=CDC73; Synonyms=C1orf28, HRPT2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11318611; DOI=10.1006/geno.2001.6500;
Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M.,
Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H.,
Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M.,
Carpten J.D.;
"Cloning and characterization of 13 novel transcripts and the human
RGS8 gene from the 1q25 region encompassing the hereditary prostate
cancer (HPC1) locus.";
Genomics 73:211-222(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-9; 38-47; 78-87; 111-120; 127-136; 172-181;
212-222; 235-243; 248-257; 332-342; 379-385 AND 400-407, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Embryonic kidney, and Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.,
Ramsay A., Leung H.Y.;
Submitted (FEB-2008) to UniProtKB.
[7]
FUNCTION, INTERACTION WITH PAF1; LEO1 AND POLR2A, INTERACTION WITH
SET1-LIKE COMPLEX, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF
VARIANT HRPT1 PRO-64.
PubMed=15632063; DOI=10.1128/MCB.25.2.612-620.2005;
Rozenblatt-Rosen O., Hughes C.M., Nannepaga S.J., Shanmugam K.S.,
Copeland T.D., Guszczynski T., Resau J.H., Meyerson M.;
"The parafibromin tumor suppressor protein is part of a human Paf1
complex.";
Mol. Cell. Biol. 25:612-620(2005).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PAF1 AND POLR2A.
PubMed=15923622; DOI=10.1128/MCB.25.12.5052-5060.2005;
Yart A., Gstaiger M., Wirbelauer C., Pecnik M., Anastasiou D.,
Hess D., Krek W.;
"The HRPT2 tumor suppressor gene product parafibromin associates with
human PAF1 and RNA polymerase II.";
Mol. Cell. Biol. 25:5052-5060(2005).
[9]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=15580289; DOI=10.1038/sj.onc.1208274;
Woodard G.E., Lin L., Zhang J.-H., Agarwal S.K., Marx S.J.,
Simonds W.F.;
"Parafibromin, product of the hyperparathyroidism-jaw tumor syndrome
gene HRPT2, regulates cyclin D1/PRAD1 expression.";
Oncogene 24:1272-1276(2005).
[10]
CHARACTERIZATION OF NUCLEAR LOCALIZATION SIGNAL.
PubMed=16116486; DOI=10.1038/sj.onc.1208778;
Hahn M.A., Marsh D.J.;
"Identification of a functional bipartite nuclear localization signal
in the tumor suppressor parafibromin.";
Oncogene 24:6241-6248(2005).
[11]
INVOLVEMENT IN HRPT2, INVOLVEMENT IN HRPT1, AND VARIANT HRPT1 PRO-64.
PubMed=12434154; DOI=10.1038/ng1048;
Carpten J.D., Robbins C.M., Villablanca A., Forsberg L.,
Presciuttini S., Bailey-Wilson J., Simonds W.F., Gillanders E.M.,
Kennedy A.M., Chen J.D., Agarwal S.K., Sood R., Jones M.P.,
Moses T.Y., Haven C., Petillo D., Leotlela P.D., Harding B.,
Cameron D., Pannett A.A., Hoeoeg A., Heath H. III, James-Newton L.A.,
Robinson B., Zarbo R.J., Cavaco B.M., Wassif W., Perrier N.D.,
Rosen I.B., Kristoffersson U., Turnpenny P.D., Farnebo L.-O.,
Besser G.M., Jackson C.E., Morreau H., Trent J.M., Thakker R.V.,
Marx S.J., Teh B.T., Larsson C., Hobbs M.R.;
"HRPT2, encoding parafibromin, is mutated in hyperparathyroidism-jaw
tumor syndrome.";
Nat. Genet. 32:676-680(2002).
[12]
INVOLVEMENT IN PRTC.
PubMed=14585940; DOI=10.1056/NEJMoa031237;
Shattuck T.M., Vaelimaeki S., Obara T., Gaz R.D., Clark O.H.,
Shoback D., Wierman M.E., Tojo K., Robbins C.M., Carpten J.D.,
Farnebo L.-O., Larsson C., Arnold A.;
"Somatic and germ-line mutations of the HRPT2 gene in sporadic
parathyroid carcinoma.";
N. Engl. J. Med. 349:1722-1729(2003).
[13]
FUNCTION.
PubMed=16989776; DOI=10.1016/j.bbrc.2006.08.169;
Zhang C., Kong D., Tan M.H., Pappas D.L. Jr., Wang P.F., Chen J.,
Farber L., Zhang N., Koo H.M., Weinreich M., Williams B.O., Teh B.T.;
"Parafibromin inhibits cancer cell growth and causes G1 phase
arrest.";
Biochem. Biophys. Res. Commun. 350:17-24(2006).
[14]
FUNCTION, AND INTERACTION WITH CTNNB1.
PubMed=16630820; DOI=10.1016/j.cell.2006.01.053;
Mosimann C., Hausmann G., Basler K.;
"Parafibromin/Hyrax activates Wnt/Wg target gene transcription by
direct association with beta-catenin/Armadillo.";
Cell 125:327-341(2006).
[15]
IDENTIFICATION IN A COMPLEX WITH BCL9L; CTNNB1 AND PYGO1.
PubMed=17113272; DOI=10.1016/j.mod.2006.09.006;
Hoffmans R., Basler K.;
"BCL9-2 binds Arm/beta-catenin in a Tyr142-independent manner and
requires Pygopus for its function in Wg/Wnt signaling.";
Mech. Dev. 124:59-67(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION IN THE PAF1 COMPLEX, AND FUNCTION OF THE PAF1 COMPLEX.
PubMed=19952111; DOI=10.1101/gad.1834709;
Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T.,
Nakamura M., Hisatake K., Handa H.;
"DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative
roles in RNA polymerase II elongation.";
Genes Dev. 23:2765-2777(2009).
[18]
FUNCTION, AND INTERACTION WITH CPSF1; CPSF4 AND CSTF2.
PubMed=19136632; DOI=10.1073/pnas.0812023106;
Rozenblatt-Rosen O., Nagaike T., Francis J.M., Kaneko S., Glatt K.A.,
Hughes C.M., LaFramboise T., Manley J.L., Meyerson M.;
"The tumor suppressor Cdc73 functionally associates with CPSF and CstF
3' mRNA processing factors.";
Proc. Natl. Acad. Sci. U.S.A. 106:755-760(2009).
[19]
FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH KMT2A.
PubMed=20541477; DOI=10.1016/j.ccr.2010.04.012;
Muntean A.G., Tan J., Sitwala K., Huang Y., Bronstein J.,
Connelly J.A., Basrur V., Elenitoba-Johnson K.S., Hess J.L.;
"The PAF complex synergizes with MLL fusion proteins at HOX loci to
promote leukemogenesis.";
Cancer Cell 17:609-621(2010).
[20]
IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX,
AND FUNCTION OF THE PAF1 COMPLEX.
PubMed=20178742; DOI=10.1016/j.cell.2009.12.050;
Kim J., Guermah M., Roeder R.G.;
"The human PAF1 complex acts in chromatin transcription elongation
both independently and cooperatively with SII/TFIIS.";
Cell 140:491-503(2010).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
FUNCTION, AND FUNCTION OF THE PAF1 COMPLEX.
PubMed=21329879; DOI=10.1016/j.molcel.2011.01.022;
Nagaike T., Logan C., Hotta I., Rozenblatt-Rosen O., Meyerson M.,
Manley J.L.;
"Transcriptional activators enhance polyadenylation of mRNA
precursors.";
Mol. Cell 41:409-418(2011).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-301, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[28]
INTERACTION WITH PTPN11, DEPHOSPHORYLATION BY PTPN11, AND
PHOSPHORYLATION.
PubMed=26742426; DOI=10.1016/j.bbrc.2015.12.117;
Noda S., Takahashi A., Hayashi T., Tanuma S., Hatakeyama M.;
"Determination of the catalytic activity of LEOPARD syndrome-
associated SHP2 mutants toward parafibromin, a bona fide SHP2
substrate involved in Wnt signaling.";
Biochem. Biophys. Res. Commun. 469:1133-1139(2016).
[29]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-198; LYS-301; LYS-308 AND
LYS-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[30]
VARIANT HRPT1 PRO-64.
PubMed=12960210; DOI=10.1136/jmg.40.9.657;
Howell V.M., Haven C.J., Kahnoski K., Khoo S.K., Petillo D., Chen J.,
Fleuren G.J., Robinson B.G., Delbridge L.W., Philips J., Nelson A.E.,
Krause U., Hammje K., Dralle H., Hoang-Vu C., Gimm O., Marsh D.J.,
Morreau H., Teh B.T.;
"HRPT2 mutations are associated with malignancy in sporadic
parathyroid tumours.";
J. Med. Genet. 40:657-663(2003).
[31]
VARIANT HRPT2 5-LEU--GLN-10 DEL, AND INVOLVEMENT IN HRPT2.
PubMed=15613436; DOI=10.1210/jc.2004-0991;
Moon S.D., Park J.H., Kim E.M., Kim J.H., Han J.H., Yoo S.J.,
Yoon K.H., Kang M.I., Lee K.W., Son H.Y., Kang S.K., Oh S.J.,
Kim K.M., Yoon S.J., Park J.G., Kim I.J., Kang H.C., Hong S.W.,
Kim K.R., Cha B.Y.;
"A Novel IVS2-1G>A mutation causes aberrant splicing of the HRPT2 gene
in a family with hyperparathyroidism-jaw tumor syndrome.";
J. Clin. Endocrinol. Metab. 90:878-883(2005).
[32]
VARIANT HRPT2 ASN-379, VARIANT HRPT1 PRO-95, AND INVOLVEMENT IN HRPT1.
PubMed=16487440; DOI=10.1111/j.1365-2265.2006.02460.x;
Bradley K.J., Cavaco B.M., Bowl M.R., Harding B., Cranston T.,
Fratter C., Besser G.M., Conceicao Pereira M., Davie M.W., Dudley N.,
Leite V., Sadler G.P., Seller A., Thakker R.V.;
"Parafibromin mutations in hereditary hyperparathyroidism syndromes
and parathyroid tumours.";
Clin. Endocrinol. (Oxf.) 64:299-306(2006).
[33]
VARIANT SER-272, AND ASSOCIATION WITH PARATHYROID ADENOMA.
PubMed=16728578; DOI=10.1677/erc.1.01058;
Juhlin C., Larsson C., Yakoleva T., Leibiger I., Leibiger B.,
Alimov A., Weber G., Hoog A., Villablanca A.;
"Loss of parafibromin expression in a subset of parathyroid
adenomas.";
Endocr. Relat. Cancer 13:509-523(2006).
[34]
VARIANT PHE-59, AND ASSOCIATION WITH PARATHYROID CARCINOMA.
PubMed=17555500; DOI=10.1111/j.1365-2265.2007.02894.x;
Haven C.J., van Puijenbroek M., Tan M.H., Teh B.T., Fleuren G.J.,
van Wezel T., Morreau H.;
"Identification of MEN1 and HRPT2 somatic mutations in paraffin-
embedded (sporadic) parathyroid carcinomas.";
Clin. Endocrinol. (Oxf.) 67:370-376(2007).
[35]
VARIANTS SER-2 AND PRO-91, AND ASSOCIATION WITH PARATHYROID ADENOMA.
PubMed=17639062; DOI=10.1677/ERC-06-0092;
Cetani F., Pardi E., Ambrogini E., Viacava P., Borsari S., Lemmi M.,
Cianferotti L., Miccoli P., Pinchera A., Arnold A., Marcocci C.;
"Different somatic alterations of the HRPT2 gene in a patient with
recurrent sporadic primary hyperparathyroidism carrying an HRPT2
germline mutation.";
Endocr. Relat. Cancer 14:493-499(2007).
[36]
VARIANTS GLN-34 AND LYS-292, CHARACTERIZATION OF VARIANT GLN-34, AND
ASSOCIATION WITH RENAL TUMORS.
PubMed=17130827; DOI=10.1038/sj.onc.1210131;
Zhao J., Yart A., Frigerio S., Perren A., Schraml P., Weisstanner C.,
Stallmach T., Krek W., Moch H.;
"Sporadic human renal tumors display frequent allelic imbalances and
novel mutations of the HRPT2 gene.";
Oncogene 26:3440-3449(2007).
[37]
VARIANT HRPT1 PRO-63, AND INVOLVEMENT IN HRPT1.
PubMed=18755853; DOI=10.1677/ERC-08-0066;
Masi G., Barzon L., Iacobone M., Viel G., Porzionato A., Macchi V.,
De Caro R., Favia G., Palu G.;
"Clinical, genetic, and histopathologic investigation of CDC73-related
familial hyperparathyroidism.";
Endocr. Relat. Cancer 15:1115-1126(2008).
-!- FUNCTION: Tumor suppressor probably involved in transcriptional
and post-transcriptional control pathways. May be involved in cell
cycle progression through the regulation of cyclin D1/PRAD1
expression. Component of the PAF1 complex (PAF1C) which has
multiple functions during transcription by RNA polymerase II and
is implicated in regulation of development and maintenance of
embryonic stem cell pluripotency. PAF1C associates with RNA
polymerase II through interaction with POLR2A CTD non-
phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and
is involved in transcriptional elongation, acting both
indepentently and synergistically with TCEA1 and in cooperation
with the DSIF complex and HTATSF1. PAF1C is required for
transcription of Hox and Wnt target genes. PAF1C is involved in
hematopoiesis and stimulates transcriptional activity of
KMT2A/MLL1; it promotes leukemogenesis through association with
KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9
and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone
modifications such as ubiquitination of histone H2B and
methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the
RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme
UBE2A or UBE2B to chromatin which mediate monoubiquitination of
'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
ubiquitination is proposed to be coupled to transcription. PAF1C
is involved in mRNA 3' end formation probably through association
with cleavage and poly(A) factors. In case of infection by
influenza A strain H3N2, PAF1C associates with viral NS1 protein,
thereby regulating gene transcription. Connects PAF1C with the
cleavage and polyadenylation specificity factor (CPSF) complex and
the cleavage stimulation factor (CSTF) complex, and with Wnt
signaling. Involved in polyadenylation of mRNA precursors.
{ECO:0000269|PubMed:15580289, ECO:0000269|PubMed:15632063,
ECO:0000269|PubMed:15923622, ECO:0000269|PubMed:16630820,
ECO:0000269|PubMed:16989776, ECO:0000269|PubMed:19136632,
ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742,
ECO:0000269|PubMed:20541477, ECO:0000269|PubMed:21329879}.
-!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73,
PAF1, LEO1, CTR9, RTF1 and WDR61 (PubMed:19952111,
PubMed:20178742). The PAF1 complex interacts with PHF5A. Within
the PAF1 complex interacts directly with PHF5A (By similarity).
Interacts with POLR2A, CPSF1, CPSF4, CSTF2, KMT2A/MLL1 and CTNNB1
(PubMed:15632063, PubMed:15923622, PubMed:16630820,
PubMed:19136632, PubMed:20541477). Interacts with a Set1-like
complex that has histone methyltransferase activity and methylates
histone H3 (PubMed:15632063). Found in a complex with BCL9L or
BCL9, CDC73, CTNNB1 and PYGO1 indicative for the participation in
a nuclear Wnt signaling complex (PubMed:17113272). Interacts with
PTPN11 (PubMed:26742426). Interacts with SETD5 (By similarity).
{ECO:0000250|UniProtKB:Q8JZM7, ECO:0000269|PubMed:15632063,
ECO:0000269|PubMed:15923622, ECO:0000269|PubMed:16630820,
ECO:0000269|PubMed:17113272, ECO:0000269|PubMed:19136632,
ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742,
ECO:0000269|PubMed:20541477, ECO:0000269|PubMed:26742426}.
-!- INTERACTION:
P13196:ALAS1; NbExp=8; IntAct=EBI-930143, EBI-3905054;
O00512:BCL9; NbExp=2; IntAct=EBI-930143, EBI-533127;
Q8N6L0:CCDC155; NbExp=6; IntAct=EBI-930143, EBI-749265;
Q8NHQ1:CEP70; NbExp=9; IntAct=EBI-930143, EBI-739624;
O95639:CPSF4; NbExp=3; IntAct=EBI-930143, EBI-725860;
P33240:CSTF2; NbExp=5; IntAct=EBI-930143, EBI-711360;
P35222:CTNNB1; NbExp=9; IntAct=EBI-930143, EBI-491549;
Q6PD62:CTR9; NbExp=19; IntAct=EBI-930143, EBI-1019583;
A1L4K1:FSD2; NbExp=8; IntAct=EBI-930143, EBI-5661036;
Q08379:GOLGA2; NbExp=10; IntAct=EBI-930143, EBI-618309;
O75031:HSF2BP; NbExp=3; IntAct=EBI-930143, EBI-7116203;
Q03164:KMT2A; NbExp=4; IntAct=EBI-930143, EBI-591370;
Q8WVC0:LEO1; NbExp=15; IntAct=EBI-930143, EBI-932432;
Q5JR59:MTUS2; NbExp=5; IntAct=EBI-930143, EBI-742948;
Q5JR59-3:MTUS2; NbExp=5; IntAct=EBI-930143, EBI-11522433;
Q8N7H5:PAF1; NbExp=27; IntAct=EBI-930143, EBI-2607770;
Q9NRD5:PICK1; NbExp=4; IntAct=EBI-930143, EBI-79165;
P24928:POLR2A; NbExp=6; IntAct=EBI-930143, EBI-295301;
Q92541:RTF1; NbExp=12; IntAct=EBI-930143, EBI-1055239;
Q12800:TFCP2; NbExp=8; IntAct=EBI-930143, EBI-717422;
Q9BZW7:TSGA10; NbExp=8; IntAct=EBI-930143, EBI-744794;
Q9H9H4:VPS37B; NbExp=3; IntAct=EBI-930143, EBI-4400866;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15580289,
ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:15923622}.
-!- TISSUE SPECIFICITY: Found in adrenal and parathyroid glands,
kidney and heart. {ECO:0000269|PubMed:15580289}.
-!- PTM: Phosphorylated. Dephosphorylated by PTPN11.
{ECO:0000269|PubMed:26742426}.
-!- DISEASE: Hyperparathyroidism 1 (HRPT1) [MIM:145000]: An autosomal
dominant disorder characterized by hypercalcemia, elevated
parathyroid hormone (PTH) levels, and uniglandular or
multiglandular parathyroid hyperplasia, adenomas, and carcinomas.
{ECO:0000269|PubMed:12434154, ECO:0000269|PubMed:12960210,
ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:16487440,
ECO:0000269|PubMed:18755853}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Hyperparathyroidism 2 with jaw tumors (HRPT2)
[MIM:145001]: An autosomal dominant neoplasia syndrome
characterized by primary hyperparathyroidism, ossifying fibroma of
the maxilla and/or mandible, renal tumor, and uterine tumors. It
is associated with increased risk of parathyroid cancer.
{ECO:0000269|PubMed:12434154, ECO:0000269|PubMed:15613436,
ECO:0000269|PubMed:16487440}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Parathyroid carcinoma (PRTC) [MIM:608266]: These cancers
characteristically result in more profound clinical manifestations
of hyperparathyroidism than do parathyroid adenomas, the most
frequent cause of primary hyperparathyroidism. Early en bloc
resection of the primary tumor is the only curative treatment.
{ECO:0000269|PubMed:14585940}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- SIMILARITY: Belongs to the CDC73 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH07325.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 300.; Evidence={ECO:0000305};
Sequence=BAB15608.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CDC73ID181ch1q31.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF312865; AAG45339.1; -; mRNA.
EMBL; AK026969; BAB15608.1; ALT_INIT; mRNA.
EMBL; AK314772; BAG37309.1; -; mRNA.
EMBL; AL139133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL390863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91250.1; -; Genomic_DNA.
EMBL; BC007325; AAH07325.1; ALT_SEQ; mRNA.
EMBL; BC014351; AAH14351.2; -; mRNA.
EMBL; BC065037; AAH65037.1; -; mRNA.
CCDS; CCDS1382.1; -.
RefSeq; NP_078805.3; NM_024529.4.
UniGene; Hs.378996; -.
ProteinModelPortal; Q6P1J9; -.
SMR; Q6P1J9; -.
BioGrid; 122724; 248.
CORUM; Q6P1J9; -.
DIP; DIP-37884N; -.
IntAct; Q6P1J9; 96.
MINT; MINT-2817439; -.
STRING; 9606.ENSP00000356405; -.
iPTMnet; Q6P1J9; -.
PhosphoSitePlus; Q6P1J9; -.
BioMuta; CDC73; -.
DMDM; 74749063; -.
EPD; Q6P1J9; -.
MaxQB; Q6P1J9; -.
PaxDb; Q6P1J9; -.
PeptideAtlas; Q6P1J9; -.
PRIDE; Q6P1J9; -.
DNASU; 79577; -.
Ensembl; ENST00000367435; ENSP00000356405; ENSG00000134371.
GeneID; 79577; -.
KEGG; hsa:79577; -.
UCSC; uc001gtb.4; human.
CTD; 79577; -.
DisGeNET; 79577; -.
EuPathDB; HostDB:ENSG00000134371.9; -.
GeneCards; CDC73; -.
GeneReviews; CDC73; -.
HGNC; HGNC:16783; CDC73.
HPA; CAB016359; -.
HPA; HPA030772; -.
MalaCards; CDC73; -.
MIM; 145000; phenotype.
MIM; 145001; phenotype.
MIM; 607393; gene.
MIM; 608266; phenotype.
neXtProt; NX_Q6P1J9; -.
OpenTargets; ENSG00000134371; -.
Orphanet; 99879; Familial isolated hyperparathyroidism.
Orphanet; 99877; Familial parathyroid adenoma.
Orphanet; 99880; Hyperparathyroidism-jaw tumor syndrome.
Orphanet; 143; Parathyroid carcinoma.
PharmGKB; PA29464; -.
eggNOG; KOG3786; Eukaryota.
eggNOG; COG5157; LUCA.
GeneTree; ENSGT00390000001114; -.
HOVERGEN; HBG055033; -.
InParanoid; Q6P1J9; -.
KO; K15175; -.
OMA; KKLQGCQ; -.
OrthoDB; EOG091G0A8X; -.
PhylomeDB; Q6P1J9; -.
TreeFam; TF313016; -.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
SignaLink; Q6P1J9; -.
SIGNOR; Q6P1J9; -.
ChiTaRS; CDC73; human.
GeneWiki; CDC73; -.
GenomeRNAi; 79577; -.
PRO; PR:Q6P1J9; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134371; -.
CleanEx; HS_CDC73; -.
ExpressionAtlas; Q6P1J9; baseline and differential.
Genevisible; Q6P1J9; HS.
GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000993; F:RNA polymerase II core binding; IDA:UniProtKB.
GO; GO:0001076; F:transcription factor activity, RNA polymerase II transcription factor binding; IBA:GO_Central.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
GO; GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
GO; GO:0006378; P:mRNA polyadenylation; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:UniProtKB.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:UniProtKB.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; IMP:UniProtKB.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0034402; P:recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex; IBA:GO_Central.
GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR007852; Cdc73/Parafibromin.
InterPro; IPR031336; CDC73_C.
InterPro; IPR032041; Cdc73_N.
PANTHER; PTHR12466; PTHR12466; 1.
Pfam; PF05179; CDC73_C; 1.
Pfam; PF16050; CDC73_N; 1.
1: Evidence at protein level;
Acetylation; Cell cycle; Complete proteome; Direct protein sequencing;
Disease mutation; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Tumor suppressor; Ubl conjugation; Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
CHAIN 2 531 Parafibromin.
/FTId=PRO_0000191803.
REGION 200 531 Interaction with POLR2A and PAF1.
REGION 200 250 Interaction with CTNNB1.
{ECO:0000269|PubMed:16630820}.
MOTIF 125 139 Nuclear localization signal.
COMPBIAS 361 364 Poly-Ile.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 198 198 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 301 301 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 308 308 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 321 321 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 2 2 A -> S (found in parathyroid adenoma
samples; somatic mutation; parathyroid
adenoma samples are from a patient with
isolated hyperparathyroidism who also
carries germline mutation P-91).
{ECO:0000269|PubMed:17639062}.
/FTId=VAR_064927.
VARIANT 5 10 Missing (in HRPT2; unknown pathological
significance; found as somatic mutation
in a parathyroid carcinoma sample from a
patient who also carries a germline
mutation causing a splicing defect).
{ECO:0000269|PubMed:15613436}.
/FTId=VAR_064928.
VARIANT 34 34 K -> Q (found in a clear cell renal
carcinoma sample; somatic mutation;
unlike wild-type protein the mutant is
defective in suppressing CCND1 expression
in vivo). {ECO:0000269|PubMed:17130827}.
/FTId=VAR_064929.
VARIANT 59 59 S -> F (found in a parathyroid carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17555500}.
/FTId=VAR_064930.
VARIANT 63 63 L -> P (in HRPT1; unknown pathological
significance).
{ECO:0000269|PubMed:18755853}.
/FTId=VAR_064931.
VARIANT 64 64 L -> P (in HRPT1; does not affect
interaction with the Pfa1 complex;
dbSNP:rs121434264).
{ECO:0000269|PubMed:12434154,
ECO:0000269|PubMed:12960210,
ECO:0000269|PubMed:15632063}.
/FTId=VAR_024082.
VARIANT 91 91 R -> P (found in a patient with isolated
hyperparathyroidism and parathyroid
adenomas). {ECO:0000269|PubMed:17639062}.
/FTId=VAR_064932.
VARIANT 95 95 L -> P (in HRPT1; unknown pathological
significance; found as somatic mutation
in a parathyroid adenoma sample from a
patient who also carries a germline
frameshift mutation).
{ECO:0000269|PubMed:16487440}.
/FTId=VAR_064933.
VARIANT 272 272 N -> S (found in a parathyroid adenoma
sample; dbSNP:rs752383339).
{ECO:0000269|PubMed:16728578}.
/FTId=VAR_064934.
VARIANT 292 292 R -> K (found in a Wilms tumor sample;
somatic mutation).
{ECO:0000269|PubMed:17130827}.
/FTId=VAR_064935.
VARIANT 379 379 D -> N (in HRPT2; dbSNP:rs971586985).
{ECO:0000269|PubMed:16487440}.
/FTId=VAR_064936.
VARIANT 384 384 L -> P (in dbSNP:rs35590728).
/FTId=VAR_031825.
CONFLICT 123 123 Q -> G (in Ref. 5; AAH14351).
{ECO:0000305}.
CONFLICT 184 187 AIKA -> CNQT (in Ref. 2; BAB15608).
{ECO:0000305}.
CONFLICT 372 372 I -> K (in Ref. 2; BAB15608).
{ECO:0000305}.
SEQUENCE 531 AA; 60577 MW; 894A7448DBC0E793 CRC64;
MADVLSVLRQ YNIQKKEIVV KGDEVIFGEF SWPKNVKTNY VVWGTGKEGQ PREYYTLDSI
LFLLNNVHLS HPVYVRRAAT ENIPVVRRPD RKDLLGYLNG EASTSASIDR SAPLEIGLQR
STQVKRAADE VLAEAKKPRI EDEECVRLDK ERLAARLEGH KEGIVQTEQI RSLSEAMSVE
KIAAIKAKIM AKKRSTIKTD LDDDITALKQ RSFVDAEVDV TRDIVSRERV WRTRTTILQS
TGKNFSKNIF AILQSVKARE EGRAPEQRPA PNAAPVDPTL RTKQPIPAAY NRYDQERFKG
KEETEGFKID TMGTYHGMTL KSVTEGASAR KTQTPAAQPV PRPVSQARPP PNQKKGSRTP
IIIIPAATTS LITMLNAKDL LQDLKFVPSD EKKKQGCQRE NETLIQRRKD QMQPGGTAIS
VTVPYRVVDQ PLKLMPQDWD RVVAVFVQGP AWQFKGWPWL LPDGSPVDIF AKIKAFHLKY
DEVRLDPNVQ KWDVTVLELS YHKRHLDRPV FLRFWETLDR YMVKHKSHLR F


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